ID   DXR_CHLMU               Reviewed;         379 AA.
AC   Q9PKW8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase;
DE            Short=DXP reductoisomerase;
DE            EC=1.1.1.267;
DE   AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase;
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase;
GN   Name=dxr; OrderedLocusNames=TC_0343;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction
CC       of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol
CC       4-phosphate (MEP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+)
CC       = 1-deoxy-D-xylulose 5-phosphate + NADPH.
CC   -!- COFACTOR: Divalent cation (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via
CC       DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate:
CC       step 1/6.
CC   -!- SIMILARITY: Belongs to the DXR family.
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DR   EMBL; AE002160; AAF39204.1; -; Genomic_DNA.
DR   PIR; G81712; G81712.
DR   RefSeq; NP_296721.1; -.
DR   HSSP; P45568; 1K5H.
DR   GeneID; 1246386; -.
DR   GenomeReviews; AE002160_GR; TC_0343.
DR   KEGG; cmu:TC0343; -.
DR   TIGR; TC_0343; -.
DR   HOGENOM; Q9PKW8; -.
DR   OMA; Q9PKW8; IHSMVEY.
DR   BioCyc; CMUR243161:TC_0343-MON; -.
DR   BRENDA; 1.1.1.267; 256349.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisome...; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00183; -; 1.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    379       1-deoxy-D-xylulose 5-phosphate
FT                                reductoisomerase.
FT                                /FTId=PRO_0000163629.
FT   NP_BIND       7     36       NADP (By similarity).
FT   METAL       147    147       Divalent metal cation (By similarity).
FT   METAL       149    149       Divalent metal cation (By similarity).
FT   METAL       218    218       Divalent metal cation (By similarity).
FT   BINDING     122    122       Substrate (By similarity).
FT   BINDING     149    149       Substrate (By similarity).
FT   BINDING     173    173       Substrate (By similarity).
FT   BINDING     196    196       Substrate (By similarity).
FT   BINDING     218    218       Substrate (By similarity).
SQ   SEQUENCE   379 AA;  41811 MW;  8C897289B35087BC CRC64;
     MKRLALIGST GSIGKQVLQV IREIPDAFVI ETLAAYGRNR ESLISQIREF SPRVVAVRDE
     TTYKELRKLF PHIEILSGEE GLIAVATAAS VDMTIVASSG IDALPAVMAS IQERKTIALA
     NKESLVAAGE LVTTLAKKNH VQILPIDSEH NALFQCLEGR DPSTIKKLIL TASGGPLRNK
     SKEELQKVTL QEVLKHPIWD MGPKITVDSS TLVNKGLEII EAFWLFGLQA VEIEAVIHPQ
     SLIHGMVEFC DGTILSVMNP PSMLFPIQHV LTFPDRYPSI ISGLNFLTNQ TLEFLPIDDE
     RFPSIRLAKD VLREGGSMGC FFNGANEALV QRFLSGEIAW YQIVSKLQTL MDKYVVRSCL
     SLEDILQVDS EARALASEC
//